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Information on EC 2.5.1.6 - methionine adenosyltransferase and Organism(s) Methanocaldococcus jannaschii and UniProt Accession Q58605

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Methanocaldococcus jannaschii
UNIPROT: Q58605 not found.
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Word Map
  • 2.5.1.6
  • monolayers
  • self-assembled
  • gold
  • film
  • alkanethiols
  • photoelectron
  • infrared
  • fabric
  • electrode
  • electrochemical
  • tunnel
  • voltammetry
  • coverage
  • interfacial
  • ellipsometry
  • impedance
  • s-adenosylhomocysteine
  • thiolate
  • silicon
  • photoemission
  • electrochemistry
  • well-ordered
  • photovoltaic
  • wafer
  • large-area
  • transistor
  • transmethylation
  • semiconductor
  • nanoscopic
  • field-effect
  • close-packed
  • stamp
  • photolithography
  • wettabl
  • nanopatterns
  • polycrystalline
  • electroless
  • thin-film
  • chemisorption
  • drug development
  • lithography
  • microcontact
  • fermi
  • headgroups
  • wettability
  • synthesis
  • medicine
  • micropatterned
  • microbalance
  • silane
  • statin-associated
  • transsulfuration
  • ferrocene
The taxonomic range for the selected organisms is: Methanocaldococcus jannaschii
The enzyme appears in selected viruses and cellular organisms
Synonyms
sams, mat2a, methionine adenosyltransferase, mat1a, s-adenosylmethionine synthetase, adomet synthetase, sam synthetase, mat ii, matalpha2, s-adenosyl-l-methionine synthetase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
adenosylmethionine synthetase
-
-
-
-
AdoMet synthetase
-
-
-
-
ATP-methionine adenosyltransferase
-
-
-
-
methionine adenosyltransferase
-
-
-
-
methionine S-adenosyltransferase
-
-
-
-
methionine-activating enzyme
-
-
-
-
S-adenosyl-L-methionine synthetase
-
-
-
-
S-adenosylmethionine synthase
-
-
-
-
S-adenosylmethionine synthetase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
adenosyl group transfer
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
ATP:L-methionine S-adenosyltransferase
-
CAS REGISTRY NUMBER
COMMENTARY hide
9012-52-6
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ATP + L-methionine + H2O
phosphate + diphosphate + S-adenosyl-L-methionine
show the reaction diagram
ITP + L-methionine + H2O
?
show the reaction diagram
-
-
-
?
2'-deoxy-ATP + L-methionine + H2O
?
show the reaction diagram
-
-
-
-
ir
3'-deoxy-ATP + L-methionine + H2O
?
show the reaction diagram
-
-
-
-
ir
ATP + D-methionine + H2O
S-adenosyl-D-methionine + phosphate + diphosphate
show the reaction diagram
-
-
-
?
ATP + L-ethionine + H2O
S-adenosyl-L-ethionine + phosphate + diphosphate
show the reaction diagram
-
-
-
?
ATP + L-methionine + H2O
S-adenosyl-L-methionine + phosphate + diphosphate
show the reaction diagram
-
-
-
ir
ATP + L-methionine methyl ester + H2O
S-adenosyl-L-methionine methyl ester + phosphate + diphosphate
show the reaction diagram
-
-
-
?
CTP + L-methionine + H2O
S-cytosyl-L-methionine + phosphate + diphosphate
show the reaction diagram
-
-
-
?
GTP + L-methionine + H2O
S-guanosyl-L-methionine + phosphate + diphosphate
show the reaction diagram
-
-
-
?
UTP + L-methionine + H2O
S-urasyl-L-methionine + phosphate + diphosphate
show the reaction diagram
-
-
-
?
additional information
?
-
-
no activity with methional, methioninol, 3-methylthiopropylamine
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
ATP + L-methionine + H2O
phosphate + diphosphate + S-adenosyl-L-methionine
show the reaction diagram
biosynthesis of S-adenosyl-L-methionine
-
-
?
ATP + L-methionine + H2O
S-adenosyl-L-methionine + phosphate + diphosphate
show the reaction diagram
-
-
-
ir
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
K+
half-maximal activation at 25 mM KCl
Mg2+
no activity is detectable in the absence of Mg2+, and maximal activity is observed at 10 mM MgCl2 when ATP is present at 5 mM, indicating that MgATP is probably the true substrate
K+
-
enhances Kcat and decrees Km values for both substrates
Mg2+
-
absolute requirement
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
GTP
-
competitive with respect to ATP and noncompetitive with L-methionine
L-ethionine
-
competitive with respect to methionine for S-adenosylmethionine formation and noncompetitive with respect to ATP
phosphate
-
competitive toward both ATP and methionine
S-adenosylmethionine
-
noncompetitive inhibitor with respect to ATP and methionine
additional information
-
no inhibition with cycloleucine, L-homocysteine, L-norleucine, L-cis-2-amino-4-methoxy-3-butenoic acid, S-adenosylhomocysteine, 5'-methylthioadenosine, sinefungin
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.1 - 0.25
ATP
0.13 - 1
L-methionine
0.22 - 1.4
ATP
3.5
D-methionine
-
-
0.74
L-ethionine
-
-
0.24 - 1.1
L-methionine
2.6
L-methionine methyl esther
-
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1 - 7.24
L-methionine
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
70
-
optimal growth temperature for Methanococcus jannaschii: 87°C
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
the enzyme is involved in biosynthesis of S-adenosyl-L-methionine
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
86000
-
recombinant enzyme, gel filtration
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
construction of a 3D-homology model. This model predicts preservation of the chain topology and three-domain organization typical of this family, locates the least stable structural elements at the flat contact surface between monomers, and shows that alterations in all three domains are required for dimer dissociation
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
W387F
W387F/Y120W
W387F/Y170W
W387F/Y226W
W387F/Y233W
W387F/Y255W
W387F/Y267W
W387F/Y273W
W387F/Y323W
W387F/Y344W
W387F/Y371W
W387F/Y49W
W387F/Y72W
W387F/Y85W
ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
guanidine-HCl
the enzyme is fully and irreversibly unfolded in the presence of guanidinium chloride. Unfolding of this dimeric protein is a three-state process in which a dimeric intermediate can be identified. The less stable secondary structural elements of the protein are the C-terminal ends of beta-strands E2 and E6
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant enzyme purified by a method that includes Ni2+-His binding resin, HiLoad Q-Sepharose and Sephadex-200 chromatography
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
expressed in Escherichia coli BL21(DE3)codon plus/pMJ1208-strain with a decahistidine tag on the N-terminus
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Lu, Z.J.; Markham, G.D.
Enzymatic properties of S-adenosylmethionine synthetase from the archaeon Methanococcus jannaschii
J. Biol. Chem.
277
16624-16631
2002
Methanocaldococcus jannaschii
Manually annotated by BRENDA team
Garrido, F.; Alfonso, C.; Taylor, J.C.; Markham, G.D.; Pajares, M.A.
Subunit association as the stabilizing determinant for archaeal methionine adenosyltransferases
Biochim. Biophys. Acta
1794
1082-1090
2009
Methanocaldococcus jannaschii (Q58605), Methanocaldococcus jannaschii
Manually annotated by BRENDA team
Garrido, F.; Taylor, J.C.; Alfonso, C.; Markham, G.D.; Pajares, M.A.
Structural basis for the stability of a thermophilic methionine adenosyltransferase against guanidinium chloride
Amino Acids
42
361-373
2010
Methanocaldococcus jannaschii (Q58605), Methanocaldococcus jannaschii, Methanocaldococcus jannaschii DSM 2661 (Q58605)
Manually annotated by BRENDA team
Graham, D.E.; Bock, C.L.; Schalk-Hihi, C.; Lu, Z.J.; Markham, G.D.
Identification of a highly diverged class of S-adenosylmethionine synthetases in the archaea
J. Biol. Chem.
275
4055-4059
2000
Methanocaldococcus jannaschii (Q58605), Methanocaldococcus jannaschii, Methanocaldococcus jannaschii DSM 2661 (Q58605)
Manually annotated by BRENDA team